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Yeast mitochondrial processing peptidase beta-E73Q mutant complexed with cytochrome C oxidase IV signal peptide

Analyse Yeast mitochondrial processing peptidase beta-E73Q mutant complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HR8
Type
protein
Length
3,598 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mitochondrial processing peptidase alpha subunit; Mitochondrial processing peptidase beta…
EC
3.4.24.64, 1.9.3.1
UniProt
P11914, P10507, P04037
Ligands
ZN
Pockets
20 · best druggability 0.86

Structure

x-ray diffraction · 11 distinct chains · 44% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMitochondrial processing peptidase alpha subunit (EC 3.4.24.64)protein45244% helix, 17% strandP11914
BMitochondrial processing peptidase beta subunit (EC 3.4.24.64)protein43946% helix, 20% strandP10507
CMitochondrial processing peptidase alpha subunit (EC 3.4.24.64)protein44845% helix, 17% strandP11914
D, FMitochondrial processing peptidase beta subunit (EC 3.4.24.64)protein44345% helix, 20% strandP10507
EMitochondrial processing peptidase alpha subunit (EC 3.4.24.64)protein44544% helix, 17% strandP11914
GMitochondrial processing peptidase alpha subunit (EC 3.4.24.64)protein44844% helix, 17% strandP11914
HMitochondrial processing peptidase beta subunit (EC 3.4.24.64)protein44146% helix, 20% strandP10507
OCytochrome C oxidase polypeptide IV (EC 1.9.3.1)protein130% helix, 23% strandP04037
PCytochrome C oxidase polypeptide IV (EC 1.9.3.1)protein90% helix, 33% strandP04037
QCytochrome C oxidase polypeptide IV (EC 1.9.3.1)protein100% helix, 30% strandP04037
RCytochrome C oxidase polypeptide IV (EC 1.9.3.1)protein70% helix, 29% strandP04037

Ligands and binding sites

  • ZN · Zinc ion · metal · 4 copies · chains B, D, F, H, R
  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, E, G

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111530.860.87135EPE
26510.800.8540empty
36090.710.7968empty
47480.710.7789empty
5790.700.9523empty

Interfaces

15 interfaces between chains.

  • C–D · 1753 Ų buried · 19 hydrogen bonds · protein-protein
  • A–B · 1678 Ų buried · 23 hydrogen bonds · protein-protein
  • E–F · 1634 Ų buried · 19 hydrogen bonds · protein-protein
  • G–H · 1572 Ų buried · 19 hydrogen bonds · protein-protein
  • A–E · 1299 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 1HR8 · Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Cytochrome C… · the same entry in another collection · chain R against R, TM-score 1.00

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